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Merck

A2290

Anti-Human IgG (γ-chain specific), F(ab′)2 fragment−Peroxidase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
Conjugate:
peroxidase conjugate
Clone:
polyclonal
Application:
ELISA (d), WB
Citations:
24
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biological source

goat

conjugate

peroxidase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

direct ELISA: 1:10,000, western blot: suitable

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

General description

Human IgGs are glycoprotein antibodies that contain two equivalent light chains and a pair of identical heavy chains. IgGs have four distinct isoforms, ranging from IgG1 to IgG4. These antibodies regulate immunological responses to allergy and pathogenic infections. IgGs have also been implicated in complement fixation and autoimmune disorders . Anti-Human IgG (γ-chain specific), (F(ab′)2) fragment-Peroxidase antibody is specific for human IgG when tested against human IgA, IgG, IgM, Bence Jones κ, and λ myeloma proteins.

Immunogen

Purified human IgG

Application

Anti-Human IgG (γ-chain specific), (F(ab′)2) fragment-Peroxidase antibody is suitable for use in ELISA and western blot .
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)
Peroxidase-conjugated goat anti-human IgG (Fab specific) antibody was used for western blot and ELISA analysis of yeast cultures genetically modified to produced recombinant Fab fragments. Anti-Human IgG antibody was used at a 1:10,000 dilution in PBS and incubated for 1 hour at room temperature. Binding in ELISA assays was detected with a O-phenylene- diamine substrate solution (Sigma).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4 containing 1% bovine serum albumin with preservative

Preparation Note

Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, Elsevier/North Holland Biomedical Press, Amsterdam, p215 (1978).

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Warning

Hazard Classifications

Aquatic Chronic 2 - Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Baik, et al.
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Ruth Thom et al.
The Lancet. Infectious diseases, 21(4), 507-516 (2020-10-17)
The 2013-16 Ebola virus disease epidemic in west Africa caused international alarm due to its rapid and extensive spread resulting in a significant death toll and social unrest within the affected region. The large number of cases provided an opportunity
K Kiernan et al.
American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons, 8(9), 1829-1839 (2008-08-02)
Antibodies directed at non-gal xenoantigens are responsible for acute humoral xenograft rejection when gal knockout (GalTKO) pig organs are transplanted into nonhuman primates. We generated IgM and IgG gene libraries using peripheral blood lymphocytes of rhesus monkeys initiating active xenoantibody
Junzo Nojima et al.
Clinical chemistry, 51(3), 545-552 (2005-01-08)
Venous thromboembolic events such as deep vein thrombosis and pulmonary embolism are common manifestations of antiphospholipid syndrome. Our aim was to clarify the roles of anti-phospholipid (aPL) antibodies in the pathogenesis of venous thromboembolism (VTE) in patients with systemic lupus
Joanne L Zahorsky-Reeves et al.
Xenotransplantation, 14(2), 135-144 (2007-03-27)
Recent work has indicated a role for anti-Gal alpha 1-3Gal (Gal) and anti-non-Gal xenoantibodies in the primate humoral rejection response against human-decay accelerating factor (hDAF) transgenic pig organs. Our laboratory has shown that anti-porcine xenograft antibodies in humans and non-human

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